Structural highlights
Publication Abstract from PubMed
Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic alpha-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.
An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.,Gouttenoire J, Montserret R, Kennel A, Penin F, Moradpour D J Virol. 2009 Nov;83(21):11378-84. Epub 2009 Aug 19. PMID:19692468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gouttenoire J, Montserret R, Kennel A, Penin F, Moradpour D. An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association. J Virol. 2009 Nov;83(21):11378-84. Epub 2009 Aug 19. PMID:19692468 doi:10.1128/JVI.01122-09